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Database: PDB
Entry: 4O68
LinkDB: 4O68
Original site: 4O68 
HEADER    TRANSFERASE                             20-DEC-13   4O68              
TITLE     STRUCTURE OF HUMAN CYCLIC GMP-AMP SYNTHASE (CGAS)                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIC GMP-AMP SYNTHASE;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 147-522;                                      
COMPND   5 SYNONYM: CGAMP SYNTHASE, CGAS, H-CGAS, MAB-21 DOMAIN-CONTAINING      
COMPND   6 PROTEIN 1;                                                           
COMPND   7 EC: 2.7.7.86;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MB21D1, C6ORF150;                                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    IMMUNE RESPONSES, TRANSFERASE                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.ZHANG,Z.CHEN,X.W.ZHANG,Z.J.CHEN                                     
REVDAT   2   05-MAR-14 4O68    1       JRNL                                     
REVDAT   1   05-FEB-14 4O68    0                                                
JRNL        AUTH   X.ZHANG,J.WU,F.DU,H.XU,L.SUN,Z.CHEN,C.A.BRAUTIGAM,X.ZHANG,   
JRNL        AUTH 2 Z.J.CHEN                                                     
JRNL        TITL   THE CYTOSOLIC DNA SENSOR CGAS FORMS AN OLIGOMERIC COMPLEX    
JRNL        TITL 2 WITH DNA AND UNDERGOES SWITCH-LIKE CONFORMATIONAL CHANGES IN 
JRNL        TITL 3 THE ACTIVATION LOOP.                                         
JRNL        REF    CELL REP                      V.   6   421 2014              
JRNL        REFN                   ESSN 2211-1247                               
JRNL        PMID   24462292                                                     
JRNL        DOI    10.1016/J.CELREP.2014.01.003                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.44 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.2_1309)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.44                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.67                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 87.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 15270                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.184                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.950                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 908                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 39.6802 -  4.4251    0.94     2735   150  0.1772 0.2107        
REMARK   3     2  4.4251 -  3.5130    0.98     2661   193  0.1546 0.2234        
REMARK   3     3  3.5130 -  3.0691    0.98     2649   169  0.1844 0.2519        
REMARK   3     4  3.0691 -  2.7886    0.99     2650   178  0.2022 0.2924        
REMARK   3     5  2.7886 -  2.5887    0.94     2524   151  0.2129 0.2901        
REMARK   3     6  2.5887 -  2.4361    0.43     1143    67  0.2066 0.3097        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.280            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.070           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           2960                                  
REMARK   3   ANGLE     :  1.251           3969                                  
REMARK   3   CHIRALITY :  0.090            431                                  
REMARK   3   PLANARITY :  0.005            502                                  
REMARK   3   DIHEDRAL  : 16.099           1141                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resid 162 through 287 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -24.5088   0.5810 -27.9380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2444 T22:  -0.0105                                     
REMARK   3      T33:   0.1182 T12:   0.0417                                     
REMARK   3      T13:  -0.0712 T23:   0.0710                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0423 L22:   0.0065                                     
REMARK   3      L33:   0.0385 L12:  -0.0003                                     
REMARK   3      L13:   0.0259 L23:  -0.0066                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0484 S12:   0.0124 S13:  -0.0946                       
REMARK   3      S21:  -0.1189 S22:  -0.0118 S23:   0.0821                       
REMARK   3      S31:  -0.0862 S32:  -0.0728 S33:   0.0103                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resid 288 through 326 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -33.6918  -5.5484 -28.8070              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1173 T22:   0.1331                                     
REMARK   3      T33:   0.1666 T12:  -0.0841                                     
REMARK   3      T13:  -0.0625 T23:  -0.0036                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0068 L22:   0.0054                                     
REMARK   3      L33:   0.0051 L12:   0.0003                                     
REMARK   3      L13:   0.0035 L23:  -0.0032                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0070 S12:   0.0002 S13:  -0.0035                       
REMARK   3      S21:   0.0033 S22:  -0.0169 S23:   0.0078                       
REMARK   3      S31:   0.0093 S32:  -0.0106 S33:  -0.0035                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resid 327 through 405 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -13.6205   7.0306 -17.5288              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1111 T22:   0.0125                                     
REMARK   3      T33:   0.1232 T12:   0.0134                                     
REMARK   3      T13:   0.0076 T23:   0.0185                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0296 L22:   0.0125                                     
REMARK   3      L33:   0.0907 L12:   0.0094                                     
REMARK   3      L13:  -0.0467 L23:  -0.0064                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0026 S12:  -0.0308 S13:  -0.0517                       
REMARK   3      S21:  -0.0838 S22:  -0.0170 S23:  -0.0359                       
REMARK   3      S31:  -0.0741 S32:   0.0213 S33:   0.0079                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'A' and (resid 406 through 519 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -25.7385   7.8480  -3.5876              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0331 T22:   0.2188                                     
REMARK   3      T33:   0.0855 T12:   0.1297                                     
REMARK   3      T13:  -0.0069 T23:   0.0978                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0387 L22:   0.0101                                     
REMARK   3      L33:   0.0167 L12:   0.0125                                     
REMARK   3      L13:   0.0050 L23:  -0.0001                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0030 S12:  -0.1306 S13:  -0.0416                       
REMARK   3      S21:   0.0196 S22:   0.0497 S23:   0.0564                       
REMARK   3      S31:  -0.1001 S32:  -0.1818 S33:   0.0652                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4O68 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JAN-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB084093.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-MAR-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97899                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16956                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 6% PEG 3,350, 0.1 M HEPES, PH 7.8,       
REMARK 280  0.05 M NACL, 0.01 M MGCL2, VAPOR DIFFUSION, HANGING DROP,           
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       81.09700            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       23.52550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       81.09700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       23.52550            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 729  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     PRO A   147                                                      
REMARK 465     VAL A   148                                                      
REMARK 465     SER A   149                                                      
REMARK 465     ALA A   150                                                      
REMARK 465     PRO A   151                                                      
REMARK 465     ILE A   152                                                      
REMARK 465     LEU A   153                                                      
REMARK 465     VAL A   154                                                      
REMARK 465     ARG A   155                                                      
REMARK 465     ARG A   156                                                      
REMARK 465     ASP A   157                                                      
REMARK 465     ALA A   158                                                      
REMARK 465     ALA A   159                                                      
REMARK 465     PRO A   160                                                      
REMARK 465     GLY A   161                                                      
REMARK 465     LYS A   254                                                      
REMARK 465     ARG A   255                                                      
REMARK 465     ASN A   256                                                      
REMARK 465     PRO A   257                                                      
REMARK 465     LYS A   258                                                      
REMARK 465     ASP A   520                                                      
REMARK 465     GLU A   521                                                      
REMARK 465     PHE A   522                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD1  ASP A   227     O    HOH A   744              2.11            
REMARK 500   O    HOH A   748     O    HOH A   761              2.12            
REMARK 500   O    HOH A   753     O    HOH A   759              2.14            
REMARK 500   O    HOH A   731     O    HOH A   774              2.14            
REMARK 500   O    HOH A   756     O    HOH A   767              2.16            
REMARK 500   O    HOH A   750     O    HOH A   764              2.18            
REMARK 500   O    HOH A   776     O    HOH A   785              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 244       -4.65     68.11                                   
REMARK 500    ALA A 307     -170.76    -66.44                                   
REMARK 500    GLU A 314       49.72     37.60                                   
REMARK 500    LYS A 315      -49.41   -156.41                                   
REMARK 500    TRP A 343      -78.19   -108.27                                   
REMARK 500    ASN A 368     -177.64   -170.46                                   
REMARK 500    GLU A 373       57.79   -104.50                                   
REMARK 500    ASN A 389       59.28   -146.28                                   
REMARK 500    PHE A 516       70.38     55.60                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    HIS A 363        23.8      L          L   OUTSIDE RANGE           
REMARK 500    PHE A 370        24.3      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 601  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 390   NE2                                                    
REMARK 620 2 CYS A 397   SG  106.6                                              
REMARK 620 3 CYS A 404   SG  101.3 114.4                                        
REMARK 620 4 CYS A 396   SG  109.0 124.5  98.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 601                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4O67   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4O6A   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4O69   RELATED DB: PDB                                   
DBREF  4O68 A  147   522  UNP    Q8N884   CGAS_HUMAN     147    522             
SEQRES   1 A  376  PRO VAL SER ALA PRO ILE LEU VAL ARG ARG ASP ALA ALA          
SEQRES   2 A  376  PRO GLY ALA SER LYS LEU ARG ALA VAL LEU GLU LYS LEU          
SEQRES   3 A  376  LYS LEU SER ARG ASP ASP ILE SER THR ALA ALA GLY MET          
SEQRES   4 A  376  VAL LYS GLY VAL VAL ASP HIS LEU LEU LEU ARG LEU LYS          
SEQRES   5 A  376  CYS ASP SER ALA PHE ARG GLY VAL GLY LEU LEU ASN THR          
SEQRES   6 A  376  GLY SER TYR TYR GLU HIS VAL LYS ILE SER ALA PRO ASN          
SEQRES   7 A  376  GLU PHE ASP VAL MET PHE LYS LEU GLU VAL PRO ARG ILE          
SEQRES   8 A  376  GLN LEU GLU GLU TYR SER ASN THR ARG ALA TYR TYR PHE          
SEQRES   9 A  376  VAL LYS PHE LYS ARG ASN PRO LYS GLU ASN PRO LEU SER          
SEQRES  10 A  376  GLN PHE LEU GLU GLY GLU ILE LEU SER ALA SER LYS MET          
SEQRES  11 A  376  LEU SER LYS PHE ARG LYS ILE ILE LYS GLU GLU ILE ASN          
SEQRES  12 A  376  ASP ILE LYS ASP THR ASP VAL ILE MET LYS ARG LYS ARG          
SEQRES  13 A  376  GLY GLY SER PRO ALA VAL THR LEU LEU ILE SER GLU LYS          
SEQRES  14 A  376  ILE SER VAL ASP ILE THR LEU ALA LEU GLU SER LYS SER          
SEQRES  15 A  376  SER TRP PRO ALA SER THR GLN GLU GLY LEU ARG ILE GLN          
SEQRES  16 A  376  ASN TRP LEU SER ALA LYS VAL ARG LYS GLN LEU ARG LEU          
SEQRES  17 A  376  LYS PRO PHE TYR LEU VAL PRO LYS HIS ALA LYS GLU GLY          
SEQRES  18 A  376  ASN GLY PHE GLN GLU GLU THR TRP ARG LEU SER PHE SER          
SEQRES  19 A  376  HIS ILE GLU LYS GLU ILE LEU ASN ASN HIS GLY LYS SER          
SEQRES  20 A  376  LYS THR CYS CYS GLU ASN LYS GLU GLU LYS CYS CYS ARG          
SEQRES  21 A  376  LYS ASP CYS LEU LYS LEU MET LYS TYR LEU LEU GLU GLN          
SEQRES  22 A  376  LEU LYS GLU ARG PHE LYS ASP LYS LYS HIS LEU ASP LYS          
SEQRES  23 A  376  PHE SER SER TYR HIS VAL LYS THR ALA PHE PHE HIS VAL          
SEQRES  24 A  376  CYS THR GLN ASN PRO GLN ASP SER GLN TRP ASP ARG LYS          
SEQRES  25 A  376  ASP LEU GLY LEU CYS PHE ASP ASN CYS VAL THR TYR PHE          
SEQRES  26 A  376  LEU GLN CYS LEU ARG THR GLU LYS LEU GLU ASN TYR PHE          
SEQRES  27 A  376  ILE PRO GLU PHE ASN LEU PHE SER SER ASN LEU ILE ASP          
SEQRES  28 A  376  LYS ARG SER LYS GLU PHE LEU THR LYS GLN ILE GLU TYR          
SEQRES  29 A  376  GLU ARG ASN ASN GLU PHE PRO VAL PHE ASP GLU PHE              
HET     ZN  A 601       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  HOH   *90(H2 O)                                                     
HELIX    1   1 ALA A  162  SER A  175  1                                  14    
HELIX    2   2 THR A  181  ASP A  200  1                                  20    
HELIX    3   3 SER A  201  ARG A  204  5                                   4    
HELIX    4   4 ASN A  260  GLN A  264  5                                   5    
HELIX    5   5 SER A  272  ILE A  288  1                                  17    
HELIX    6   6 PRO A  331  GLN A  335  5                                   5    
HELIX    7   7 SER A  345  ARG A  353  1                                   9    
HELIX    8   8 PHE A  379  ASN A  388  1                                  10    
HELIX    9   9 CYS A  405  PHE A  424  1                                  20    
HELIX   10  10 SER A  434  ASN A  449  1                                  16    
HELIX   11  11 GLN A  451  LYS A  458  5                                   8    
HELIX   12  12 ASP A  459  THR A  477  1                                  19    
HELIX   13  13 ASP A  497  ASN A  514  1                                  18    
SHEET    1   A 7 VAL A 206  LEU A 208  0                                        
SHEET    2   A 7 GLU A 225  GLU A 233 -1  O  LYS A 231   N  GLY A 207           
SHEET    3   A 7 ILE A 316  SER A 326  1  O  ASP A 319   N  VAL A 228           
SHEET    4   A 7 PHE A 357  PRO A 361 -1  O  LEU A 359   N  LEU A 324           
SHEET    5   A 7 TRP A 375  SER A 378 -1  O  ARG A 376   N  VAL A 360           
SHEET    6   A 7 TYR A 248  LYS A 252 -1  N  TYR A 249   O  TRP A 375           
SHEET    7   A 7 GLN A 238  GLU A 241 -1  N  GLN A 238   O  LYS A 252           
SHEET    1   B 5 VAL A 206  LEU A 208  0                                        
SHEET    2   B 5 GLU A 225  GLU A 233 -1  O  LYS A 231   N  GLY A 207           
SHEET    3   B 5 ILE A 316  SER A 326  1  O  ASP A 319   N  VAL A 228           
SHEET    4   B 5 VAL A 308  ILE A 312 -1  N  ILE A 312   O  ILE A 316           
SHEET    5   B 5 VAL A 296  LYS A 299 -1  N  ILE A 297   O  LEU A 311           
SHEET    1   C 2 LEU A 266  GLU A 267  0                                        
SHEET    2   C 2 ILE A 270  LEU A 271 -1  O  ILE A 270   N  GLU A 267           
LINK         NE2 HIS A 390                ZN    ZN A 601     1555   1555  2.16  
LINK         SG  CYS A 397                ZN    ZN A 601     1555   1555  2.33  
LINK         SG  CYS A 404                ZN    ZN A 601     1555   1555  2.36  
LINK         SG  CYS A 396                ZN    ZN A 601     1555   1555  2.46  
CISPEP   1 ARG A  302    GLY A  303          0         2.43                     
CISPEP   2 ALA A  364    LYS A  365          0        -5.70                     
CISPEP   3 GLY A  369    PHE A  370          0        22.28                     
SITE     1 AC1  4 HIS A 390  CYS A 396  CYS A 397  CYS A 404                    
CRYST1  162.194   47.051   58.404  90.00  90.00  90.00 P 21 21 2     4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006165  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.021254  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017122        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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